Vasodilator-stimulated phosphoprotein

VASP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1EGX, 1USD, 1USE, 2PAV, 2PBD, 3CHW
Identifiers
Aliases	VASP, vasodilator-stimulated phosphoprotein, vasodilator stimulated phosphoprotein
External IDs	OMIM: 601703 MGI: 109268 HomoloGene: 7592 GeneCards: VASP
Gene location (Human)
Chr.	Chromosome 19 (human)
End	45,526,983 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	19,005,742 bp
RNA expression pattern
	Top expressed in
	monocyte; ; saphenous vein; ; spleen; ; blood; ; rectum; ; thoracic aorta; ; ascending aorta; ; left uterine tube; ; right coronary artery; ; upper lobe of left lung;
	Top expressed in
	colon; ; spleen; ; left colon; ; left lung lobe; ; pyloric antrum; ; epithelium of stomach; ; atrium; ; duodenum; ; yolk sac; ; blood;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	profilin binding; SH3 domain binding; protein binding; actin binding; cadherin binding;
Cellular component	cell projection; membrane; focal adhesion; bicellular tight junction; filopodium; plasma membrane; cell junction; actin cytoskeleton; extracellular exosome; cytoskeleton; lamellipodium membrane; lamellipodium; filopodium membrane; cytoplasm; cytosol;
Biological process	positive regulation of actin filament polymerization; axon guidance; neural tube closure; actin polymerization or depolymerization; protein homotetramerization; actin cytoskeleton organization; cell junction assembly;
	Sources:Amigo / QuickGO
Orthologs
	7408
	22323
	ENSG00000125753
	ENSMUSG00000030403
	P50552
	P70460
	NM_001008736; NM_003370
	NM_001282021; NM_001282022; NM_009499
	NP_003361
	NP_001268950; NP_001268951; NP_033525
	Wikidata
View/Edit Human	View/Edit Mouse

Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.^[5]^[6]

Function

Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an N-terminal EVH1 domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions cell membranes. In the mid-region of the protein, family members have a proline-rich region that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.^[6]

Interactions

Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin,^[7]^[8] Profilin 1,^[7] and PFN2.^[7]^[9]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125753 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030403 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U (January 1997). "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization". Genomics. 36 (2): 227–33. doi:10.1006/geno.1996.0457. PMID 8812448.
1 2 "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
1 2 3 Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
↑ Drees, B; Friederich E; Fradelizi J; Louvard D; Beckerle M C; Golsteyn R M (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.
↑ Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN 0261-4189. PMC 398250. PMID 7737110.

Reinhard M, Halbrügge M, Scheer U, et al. (1992). "The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts". EMBO J. 11 (6): 2063–70. doi:10.1002/j.1460-2075.1992.tb05264.x. PMC 556672. PMID 1318192.
Halbrügge M, Eigenthaler M, Polke C, Walter U (1992). "Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes". Cell. Signal. 4 (2): 189–99. doi:10.1016/0898-6568(92)90082-J. PMID 1319722.
Reinhard M, Jouvenal K, Tripier D, Walter U (1995). "Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7956–60. Bibcode:1995PNAS...92.7956R. doi:10.1073/pnas.92.17.7956. PMC 41265. PMID 7644520.
Reinhard M, Giehl K, Abel K, et al. (1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. PMC 398250. PMID 7737110.
Haffner C, Jarchau T, Reinhard M, et al. (1995). "Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP". EMBO J. 14 (1): 19–27. doi:10.1002/j.1460-2075.1995.tb06971.x. PMC 398048. PMID 7828592.
Horstrup K, Jablonka B, Hönig-Liedl P, et al. (1994). "Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition". Eur. J. Biochem. 225 (1): 21–7. doi:10.1111/j.1432-1033.1994.00021.x. PMID 7925440.
Butt E, Abel K, Krieger M, et al. (1994). "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets". J. Biol. Chem. 269 (20): 14509–17. doi:10.1016/S0021-9258(17)36652-8. PMID 8182057.
Laurent V, Loisel TP, Harbeck B, et al. (1999). "Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes". J. Cell Biol. 144 (6): 1245–58. doi:10.1083/jcb.144.6.1245. PMC 2150578. PMID 10087267.
Bachmann C, Fischer L, Walter U, Reinhard M (1999). "The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation". J. Biol. Chem. 274 (33): 23549–57. doi:10.1074/jbc.274.33.23549. PMID 10438535.
Petit MM, Fradelizi J, Golsteyn RM, et al. (2000). "LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity". Mol. Biol. Cell. 11 (1): 117–29. doi:10.1091/mbc.11.1.117. PMC 14761. PMID 10637295.
Krause M, Sechi AS, Konradt M, et al. (2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096.
Drees B, Friederich E, Fradelizi J, et al. (2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
Smolenski A, Poller W, Walter U, Lohmann SM (2000). "Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I". J. Biol. Chem. 275 (33): 25723–32. doi:10.1074/jbc.M909632199. PMID 10851246.
Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
Burkhardt M, Glazova M, Gambaryan S, et al. (2000). "KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells". J. Biol. Chem. 275 (43): 33536–41. doi:10.1074/jbc.M005670200. PMID 10922374.
Ball LJ, Kühne R, Hoffmann B, et al. (2000). "Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity". EMBO J. 19 (18): 4903–14. doi:10.1093/emboj/19.18.4903. PMC 314220. PMID 10990454.
Bearer EL, Prakash JM, Manchester RD, Allen PG (2001). "VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations". Cell Motil. Cytoskeleton. 47 (4): 351–64. doi:10.1002/1097-0169(200012)47:4<351::AID-CM8>3.0.CO;2-8. PMC 3376085. PMID 11093254.
Lawrence DW, Pryzwansky KB (2001). "The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading". J. Immunol. 166 (9): 5550–6. doi:10.4049/jimmunol.166.9.5550. PMID 11313394.
Castellano F, Le Clainche C, Patin D, et al. (2001). "A WASp-VASP complex regulates actin polymerization at the plasma membrane". EMBO J. 20 (20): 5603–14. doi:10.1093/emboj/20.20.5603. PMC 125672. PMID 11598004.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000125753 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030403 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8812448-5] Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U (January 1997). "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization". Genomics. 36 (2): 227–33. doi:10.1006/geno.1996.0457. PMID 8812448.

[entrez-6] 1 2 "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".

[pmid10882740-7] 1 2 3 Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.

[pmid10801818-8] Drees, B; Friederich E; Fradelizi J; Louvard D; Beckerle M C; Golsteyn R M (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.

[pmid7737110-9] Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN 0261-4189. PMC 398250. PMID 7737110.

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Function

Interactions

References

Further reading